The atypical protein arginine methyltrasferase of Entamoeba histolytica (EhPRMTA) is involved in cell proliferation, heat shock response and in vitro virulence

Medina-Gómez, Christian; Bolaños, Jeni; Borbolla-Vázquez, Jessica; Munguía-Robledo, Susana; Orozco, Esther; Rodríguez, Mario A.

doi:10.1016/j.exppara.2021.108077

Cited by 4 publications

(3 citation statements)

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“…Cell migration of EhPKMT2-KD and mock trophozoites was performed as described [ 19 ], whereas their erythrophagocytosis rate and cytopathic effect on MDCK cells were determined as previously reported [ 20 ].…”

Section: Methodsmentioning

confidence: 99%

Lysine Methyltransferase EhPKMT2 Is Involved in the In Vitro Virulence of Entamoeba histolytica

et al. 2023

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Lysine methylation, a posttranslational modification catalyzed by protein lysine methyltransferases (PKMTs), is involved in epigenetics and several signaling pathways, including cell growth, cell migration and stress response, which in turn may participate in virulence of protozoa parasites. Entamoeba histolytica, the etiologic agent of human amebiasis, has four PKMTs (EhPKMT1 to EhPKMT4), but their role in parasite biology is unknown. Here, to obtain insight into the role of EhPKMT2, we analyzed its expression level and localization in trophozoites subjected to heat shock and during phagocytosis, two events that are related to amoeba virulence. Moreover, the effect of EhPKMT2 knockdown on those activities and on cell growth, migration and cytopathic effect was investigated. The results indicate that this enzyme participates in all these cellular events, suggesting that it could be a potential target for development of novel therapeutic strategies against amebiasis.

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Section: Methodsmentioning

confidence: 99%

Lysine Methyltransferase EhPKMT2 Is Involved in the In Vitro Virulence of Entamoeba histolytica

et al. 2023

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“…In concordance, this protein was not recognized by an antibody against human PRMT1 (Borbolla-Vázquez et al ., 2015). In addition, it does not contain several of the canonical amino acid residues of type I PRMTs (Medina-Gómez et al ., 2021) and a phylogenetic analysis grouped this protein with the inactive PRMT3 of T. brucei (Fig. 1), although the EhPRMTA recombinant protein displayed enzymatic activity on commercial histones (Medina-Gómez et al ., 2021).…”

Section: Arginine Methylation and Prmts In Protozoan Parasitesmentioning

confidence: 99%

“…In addition, it does not contain several of the canonical amino acid residues of type I PRMTs (Medina-Gómez et al ., 2021) and a phylogenetic analysis grouped this protein with the inactive PRMT3 of T. brucei (Fig. 1), although the EhPRMTA recombinant protein displayed enzymatic activity on commercial histones (Medina-Gómez et al ., 2021). On the other hand, EhPRMTA interacts with the EhTSN protein, which is a transcription factor of E. histolytica (Cázares-Apátiga et al ., 2017) and its homologues in other protozoan parasites participate in RNA metabolism (Hossain et al ., 2008; Musiyenko et al ., 2012), suggesting that this EhPRMT is involved in transcription regulation and in RNA metabolism; moreover, the EhPRMTA-knockdown increased cell growth and phagocytosis, but decreased cell migration and survival of trophozoites submitted to heat shock (Medina-Gómez et al ., 2021), indicating that this PRMT participates in these events (Table 1), although the identification of its protein targets remains to be determined.…”

Section: Arginine Methylation and Prmts In Protozoan Parasitesmentioning

confidence: 99%

Protein arginine methyltransferases in protozoan parasites

Rodríguez

2021

Parasitology

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Arginine methylation is a post-translational modification involved in gene transcription, signalling pathways, DNA repair, RNA metabolism and splicing, among others, mechanisms that in protozoa parasites may be involved in pathogenicity-related events. This modification is performed by protein arginine methyltransferases (PRMTs), which according to their products are divided into three main types: type I yields monomethylarginine (MMA) and asymmetric dimethylarginine; type II produces MMA and symmetric dimethylarginine; whereas type III catalyses MMA only. Nine PRMTs (PRMT1 to PRMT9) have been characterized in humans, whereas in protozoa parasites, except for Giardia intestinalis, three to eight PRMTs have been identified, where in each group there are at least two enzymes belonging to type I, the majority with higher similarity to human PRMT1, and one of type II, related to human PRMT5. However, the information on the role of most of these enzymes in the parasites biology is limited so far. Here, current knowledge of PRMTs in protozoan parasites is reviewed; these enzymes participate in the cell growth, stress response, stage transitions and virulence of these microorganisms. Thus, PRMTs are attractive targets for developing new therapeutic strategies against these pathogens.

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Adriamycin induces cardiac fibrosis in mice via PRMT5-mediated cardiac fibroblast activation

Dong

Yuan

et al. 2022

Acta Pharmacol Sin

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The atypical protein arginine methyltrasferase of Entamoeba histolytica (EhPRMTA) is involved in cell proliferation, heat shock response and in vitro virulence

Cited by 4 publications

References 50 publications

Lysine Methyltransferase EhPKMT2 Is Involved in the In Vitro Virulence of Entamoeba histolytica

Lysine Methyltransferase EhPKMT2 Is Involved in the In Vitro Virulence of Entamoeba histolytica

Protein arginine methyltransferases in protozoan parasites

Adriamycin induces cardiac fibrosis in mice via PRMT5-mediated cardiac fibroblast activation

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